ArticleeLife2023
Transcriptional regulation of Sis1 promotes fitness but not feedback in the heat shock response.
Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Chaperone condensates buffer the heat shock response against pleiotropic inputs.bioRxiv : the preprint server for biology · 2026Article
- Mitochondrial respiration modulates Hsf1 activation and the heat shock response.bioRxiv : the preprint server for biology · 2026Article
- Physiological architecture and evolutionary origins of cellular adaptability.bioRxiv : the preprint server for biology · 2026Article
- Article
- Co-chaperones fine-tune the function of heat shock protein 70 (Hsp70), whether to fold, hold, or degrade substrates in ensuring cellular protein homeostasis.Journal of biosciences · 2025Review
- Fine-tuning stress responses by auxiliary feedback loops that sense damage repair.The Journal of cell biology · 2024Article
- Feedback control of the heat shock response by spatiotemporal regulation of Hsp70.The Journal of cell biology · 2024Article
- Preserve or destroy: Orphan protein proteostasis and the heat shock response.The Journal of cell biology · 2024Review
- The Heat Shock Response as a Condensate Cascade.Journal of molecular biology · 2024Review
- Feedback control of the heat shock response by spatiotemporal regulation of Hsp70.bioRxiv : the preprint server for biology · 2024Article
- Adaptive preservation of orphan ribosomal proteins in chaperone-dispersed condensates.Nature cell biology · 2023Article
- Transcriptional regulation of Sis1 promotes fitness but not feedback in the heat shock response.eLife · 2023Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The heat shock response (HSR) controls expression of molecular chaperones to maintain protein homeostasis. Previously, we proposed a feedback loop model of the HSR in which heat-denatured proteins sequester the chaperone Hsp70 to activate the HSR, and subsequent induction of Hsp70 deactivates the HSR (Krakowiak et al., 2018; Zheng et al., 2016). However, recent work has implicated newly synthesized proteins (NSPs) - rather than unfolded mature proteins - and the Hsp70 co-chaperone Sis1 in HSR regulation, yet their contributions to HSR dynamics have not been determined. Here, we generate a new mathematical model that incorporates NSPs and Sis1 into the HSR activation mechanism, and we perform genetic decoupling and pulse-labeling experiments to demonstrate that Sis1 induction is dispensable for HSR deactivation. Rather than providing negative feedback to the HSR, transcriptional regulation of Sis1 by Hsf1 promotes fitness by coordinating stress granules and carbon metabolism. These results support an overall model in which NSPs signal the HSR by sequestering Sis1 and Hsp70, while induction of Hsp70 - but not Sis1 - attenuates the response.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.